Antimicrobial Properties of a Peptide Derived from the Male Fertility Factor kl2 Protein of Drosophila melanogaster.

Bernadetta Bilska,Milena Damulewicz,Elżbieta Pyza,Krzysztof Murzyn,Mateusz Kwitniewski,Urszula Godlewska,Joanna Cichy

doi:10.3390/cimb44030076

Abstract

Antimicrobial peptides (AMPs) are important components of innate immunity. Here, we report the antimicrobial properties of a peptide derived from the Male fertility factor kl2 (MFF-kl2) protein of Drosophila melanogaster, which was identified as a functional analog of the mammalian antibacterial chemerin-p4 peptide. The antimicrobial activity of multifunctional chemerin is mainly associated with a domain localized in the middle of the chemerin sequence, Val66-Pro85 peptide (chemerin-p4). Using bioinformatic tools, we found homologs of the chemerin-p4 peptide in the proteome of D. melanogaster. One of them is MFF-p1, which is a part of the MFF kl2 protein, encoded by the gene male fertility factor kl2 (kl-2) located on the long arm of the Y chromosome. The second detected peptide (Z-p1) is a part of the Zizimin protein belonging to DOCK family, which is involved in cellular signaling processes. After testing the antimicrobial properties of both peptides, we found that only MFF-p1 possesses these properties. Here, we demonstrate its antimicrobial potential both in vitro and in vivo after infecting D. melanogaster with bacteria. MFF-p1 strongly inhibits the viable counts of E. coli and B. subtilis after 2 h of treatment and disrupts bacterial cells. The expression of kl-2 is regulated by exposure to bacteria and by the circadian clock.

Highlights

Antimicrobial peptides (AMPs), known as “host-defense peptides”, exhibit antibacterial, antifungal, and antiviral potency
Analyses of the results from transmissi electron microscopy in the present study showed massive changes in the cell en lope and bacteria morphology, both in E. coli and B. subtilis strains treated with MFF
Analyses of the results from transmission electron microscopy in the present study showed massive changes in the cell envelope and bacteria morphology, both in E. coli and B. subtilis strains treated with MFF-p1

Summary

Introduction

Antimicrobial peptides (AMPs), known as “host-defense peptides”, exhibit antibacterial, antifungal, and antiviral potency. Because of the absence of adaptive immune responses in insects, AMPs are essential for insect innate immunity in fighting pathogens [2]. They are intensively studied due to their potential applications as novel antimicrobial drugs [3]. Seven well-characterized families of inducible AMPs have been identified in Drosophila melanogaster. These include: antibacterial Diptericins, Drosocins and Attacins [5–9], antifungal Drosomycins and Metchnikowin [10,11], and Cecropins and Defensin, which exhibit both antibacterial and antifungal activities [12–15]

Objectives

Methods

Results

Conclusion